SitesBLAST
Comparing Pf1N1B4_5098 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_5098 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
38% identity, 97% coverage: 1:254/263 of query aligns to 14:262/378 of P69874
- C26 (≠ H13) mutation to A: Lower ATPase activity and transport efficiency.
- F27 (= F14) mutation to L: Lower ATPase activity and transport efficiency.
- F45 (= F36) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (= C45) mutation to T: Loss of ATPase activity and transport.
- L60 (= L51) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ C67) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (= V126) mutation to M: Loss of ATPase activity and transport.
- D172 (= D163) mutation to N: Loss of ATPase activity and transport.
Sites not aligning to the query:
- 276 C→A: Lower ATPase activity and transport efficiency.
- 297 mutation E->K,D: Lower ATPase activity and transport efficiency.; E→Q: Loss of ATPase activity and transport.
7ahhC Opua inhibited inward-facing, sbd docked (see paper)
38% identity, 79% coverage: 17:225/263 of query aligns to 35:252/382 of 7ahhC
Sites not aligning to the query:
- binding (2R,3R,3aS,5R,7aR,9R,10R,10aS,12R,14aR)-2,9-bis(6-amino-9H-purin-9-yl)octahydro-2H,7H-difuro[3,2-d:3',2'-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-3,5,10,12-tetrol 5,12-dioxide: 275, 297, 298
- binding phosphoaminophosphonic acid-adenylate ester: 12
7aheC Opua inhibited inward facing (see paper)
38% identity, 79% coverage: 17:225/263 of query aligns to 35:252/382 of 7aheC
Sites not aligning to the query:
- binding (2R,3R,3aS,5R,7aR,9R,10R,10aS,12R,14aR)-2,9-bis(6-amino-9H-purin-9-yl)octahydro-2H,7H-difuro[3,2-d:3',2'-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-3,5,10,12-tetrol 5,12-dioxide: 275, 297, 298
7ahdC Opua (e190q) occluded (see paper)
37% identity, 79% coverage: 17:225/263 of query aligns to 35:252/260 of 7ahdC
- binding adenosine-5'-triphosphate: T39 (≠ F21), S61 (= S43), G62 (= G44), G64 (= G46), K65 (= K47), S66 (= S48), T67 (= T49), Q111 (= Q84), K161 (≠ S137), Q162 (≠ E138), S164 (= S140), G166 (= G142), M167 (= M143), Q188 (≠ E164), H221 (= H197)
Sites not aligning to the query:
8hprD Lpqy-sugabc in state 4 (see paper)
36% identity, 82% coverage: 7:221/263 of query aligns to 5:216/362 of 8hprD
- binding adenosine-5'-triphosphate: Y12 (≠ F14), S38 (= S43), C40 (= C45), G41 (= G46), K42 (= K47), S43 (= S48), T44 (= T49), Q82 (= Q84), R129 (≠ K134), Q133 (≠ E138), S135 (= S140), G136 (= G141), G137 (= G142), Q159 (≠ E164), H192 (= H197)
- binding magnesium ion: S43 (= S48), Q82 (= Q84)
8hprC Lpqy-sugabc in state 4 (see paper)
36% identity, 82% coverage: 7:221/263 of query aligns to 5:216/363 of 8hprC
- binding adenosine-5'-triphosphate: Y12 (≠ F14), S38 (= S43), G39 (= G44), G41 (= G46), K42 (= K47), S43 (= S48), Q82 (= Q84), Q133 (≠ E138), G136 (= G141), G137 (= G142), Q138 (≠ M143), H192 (= H197)
- binding magnesium ion: S43 (= S48), Q82 (= Q84)
P9WQI3 Trehalose import ATP-binding protein SugC; MtbSugC; Nucleotide-binding domain of SugABC transporter; NBD of SugABC transporter; SugABC transporter ATPase SugC; EC 7.5.2.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
37% identity, 76% coverage: 23:221/263 of query aligns to 19:217/393 of P9WQI3
- H193 (= H197) mutation to A: Decreased hydrolysis of ATP. No change in KM, but 2-fold reduction in Vmax compared to wild-type.
8hplC Lpqy-sugabc in state 1 (see paper)
37% identity, 78% coverage: 16:221/263 of query aligns to 9:214/384 of 8hplC
1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp (see paper)
35% identity, 85% coverage: 5:228/263 of query aligns to 7:218/353 of 1vciA
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
37% identity, 88% coverage: 5:236/263 of query aligns to 3:229/374 of 2awnB
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
37% identity, 88% coverage: 5:236/263 of query aligns to 1:227/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (≠ F14), S35 (= S43), G36 (= G44), C37 (= C45), G38 (= G46), K39 (= K47), S40 (= S48), T41 (= T49), R126 (≠ K134), A130 (≠ E138), S132 (= S140), G134 (= G142), Q135 (≠ M143)
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
37% identity, 88% coverage: 5:236/263 of query aligns to 4:230/371 of P68187
- A85 (≠ S87) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (= K108) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (≠ T119) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ A122) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ A124) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ E129) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G142) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D163) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
- R228 (= R234) mutation to C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
Sites not aligning to the query:
- 241 F→I: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- 267 W→G: Normal maltose transport but constitutive mal gene expression.
- 278 G→P: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- 282 S→L: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- 284 G→S: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- 302 G→D: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- 308 E→Q: Maltose transport is affected but retains ability to interact with MalT.
- 322 S→F: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- 340 G→A: Maltose transport is affected but retains ability to interact with MalT.
- 346 G→S: Normal maltose transport but constitutive mal gene expression.
- 355 F→Y: Maltose transport is affected but retains ability to interact with MalT.
3puyA Crystal structure of an outward-facing mbp-maltose transporter complex bound to amp-pnp after crystal soaking of the pretranslocation state (see paper)
37% identity, 88% coverage: 5:236/263 of query aligns to 3:229/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ F14), S37 (= S43), G38 (= G44), C39 (= C45), G40 (= G46), K41 (= K47), S42 (= S48), T43 (= T49), Q81 (= Q84), R128 (≠ K134), A132 (≠ E138), S134 (= S140), G136 (= G142), Q137 (≠ M143), E158 (= E164), H191 (= H197)
- binding magnesium ion: S42 (= S48), Q81 (= Q84)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
37% identity, 88% coverage: 5:236/263 of query aligns to 3:229/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ F14), G38 (= G44), C39 (= C45), G40 (= G46), K41 (= K47), S42 (= S48), T43 (= T49), R128 (≠ K134), S134 (= S140), Q137 (≠ M143)
- binding beryllium trifluoride ion: S37 (= S43), G38 (= G44), K41 (= K47), Q81 (= Q84), S134 (= S140), G136 (= G142), H191 (= H197)
- binding magnesium ion: S42 (= S48), Q81 (= Q84)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
37% identity, 88% coverage: 5:236/263 of query aligns to 3:229/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ F14), V17 (≠ A23), G38 (= G44), C39 (= C45), G40 (= G46), K41 (= K47), S42 (= S48), T43 (= T49), R128 (≠ K134), A132 (≠ E138), S134 (= S140), Q137 (≠ M143)
- binding tetrafluoroaluminate ion: S37 (= S43), G38 (= G44), K41 (= K47), Q81 (= Q84), S134 (= S140), G135 (= G141), G136 (= G142), E158 (= E164), H191 (= H197)
- binding magnesium ion: S42 (= S48), Q81 (= Q84)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
37% identity, 88% coverage: 5:236/263 of query aligns to 3:229/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ F14), V17 (≠ A23), G38 (= G44), C39 (= C45), G40 (= G46), K41 (= K47), S42 (= S48), T43 (= T49), R128 (≠ K134), A132 (≠ E138), S134 (= S140), Q137 (≠ M143)
- binding magnesium ion: S42 (= S48), Q81 (= Q84)
P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
37% identity, 88% coverage: 5:236/263 of query aligns to 4:230/369 of P19566
- L86 (= L88) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P165) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D170) mutation to N: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
Sites not aligning to the query:
- 306 E→K: Loss of transport. No effect on ATP-binding and ATP hydrolysis. Retains repressor activity.
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
35% identity, 88% coverage: 5:236/263 of query aligns to 7:239/375 of 2d62A
1g291 Malk (see paper)
33% identity, 88% coverage: 5:236/263 of query aligns to 4:236/372 of 1g291
- binding magnesium ion: D69 (≠ G74), E71 (≠ G76), K72 (vs. gap), K79 (≠ R79), D80 (vs. gap)
- binding pyrophosphate 2-: S38 (= S43), G39 (= G44), C40 (= C45), G41 (= G46), K42 (= K47), T43 (≠ S48), T44 (= T49)
Sites not aligning to the query:
3d31A Modbc from methanosarcina acetivorans (see paper)
34% identity, 79% coverage: 16:222/263 of query aligns to 8:211/348 of 3d31A
Sites not aligning to the query:
Query Sequence
>Pf1N1B4_5098 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_5098
MTKFVELTQVSKHFDTKKGRFQALSNVNLSIARGEFVSLIGHSGCGKSTVLNLIAGLLEA
NGGGLICNGREIDGPGPERAVVFQNHSLLPWLTCFGNVHLAVEKVFGKRENKAALKTRTE
AALAMVGLEHAMHKHPSEISGGMKQRVGIARALAMEPKILLMDEPFGALDALTRAHLQDE
LLRIVAATQSTVVMVTHDVDEAVLLSDRIVMMTNGPAATVGEILSVGLAKPRNRLVLAND
PEYHRYRTTVLEFLYHRQQMPAA
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SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory